Single-Cell High-Throughput Screening To Identify Enantioselective Hydrolytic Enzymes
Getting a look in: A high‐throughput screening method has been developed for the identification and isolation of enantioselective hydrolases displayed on cell surfaces (see scheme; E: Esterase, P: Peroxidase). Enantiomeric substrates labeled with two different fluorescent dyes allow real‐time analys...
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Veröffentlicht in: | Angewandte Chemie (International ed.) 2008-06, Vol.47 (27), p.5085-5088 |
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container_title | Angewandte Chemie (International ed.) |
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creator | Becker, Stefan Höbenreich, Horst Vogel, Andreas Knorr, Janina Wilhelm, Susanne Rosenau, Frank Jaeger, Karl-Erich Reetz, Manfred T Kolmar, Harald |
description | Getting a look in: A high‐throughput screening method has been developed for the identification and isolation of enantioselective hydrolases displayed on cell surfaces (see scheme; E: Esterase, P: Peroxidase). Enantiomeric substrates labeled with two different fluorescent dyes allow real‐time analysis of enantioselectivity by determination of the ratio of green and red single‐cell fluorescence. |
doi_str_mv | 10.1002/anie.200705236 |
format | Article |
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Enantiomeric substrates labeled with two different fluorescent dyes allow real‐time analysis of enantioselectivity by determination of the ratio of green and red single‐cell fluorescence.</description><identifier>ISSN: 1433-7851</identifier><identifier>EISSN: 1521-3773</identifier><identifier>DOI: 10.1002/anie.200705236</identifier><identifier>PMID: 18512207</identifier><language>eng</language><publisher>Weinheim: Wiley-VCH Verlag</publisher><subject>asymmetric catalysis ; directed evolution ; Directed Molecular Evolution ; Drug Evaluation, Preclinical ; enzyme catalysis ; Escherichia coli - enzymology ; Esterases - chemistry ; Flow Cytometry ; hydrolases ; Hydrolysis ; kinetic resolution ; Models, Biological ; Molecular Structure ; Peroxidase - chemistry ; Stereoisomerism ; Surface Properties</subject><ispartof>Angewandte Chemie (International ed.), 2008-06, Vol.47 (27), p.5085-5088</ispartof><rights>Copyright © 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4716-d33b19a857ddbd8a95d33416209f57c679ee888c7f5f044829d6d0659defc7663</citedby><cites>FETCH-LOGICAL-c4716-d33b19a857ddbd8a95d33416209f57c679ee888c7f5f044829d6d0659defc7663</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fanie.200705236$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fanie.200705236$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18512207$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Becker, Stefan</creatorcontrib><creatorcontrib>Höbenreich, Horst</creatorcontrib><creatorcontrib>Vogel, Andreas</creatorcontrib><creatorcontrib>Knorr, Janina</creatorcontrib><creatorcontrib>Wilhelm, Susanne</creatorcontrib><creatorcontrib>Rosenau, Frank</creatorcontrib><creatorcontrib>Jaeger, Karl-Erich</creatorcontrib><creatorcontrib>Reetz, Manfred T</creatorcontrib><creatorcontrib>Kolmar, Harald</creatorcontrib><title>Single-Cell High-Throughput Screening To Identify Enantioselective Hydrolytic Enzymes</title><title>Angewandte Chemie (International ed.)</title><addtitle>Angewandte Chemie International Edition</addtitle><description>Getting a look in: A high‐throughput screening method has been developed for the identification and isolation of enantioselective hydrolases displayed on cell surfaces (see scheme; E: Esterase, P: Peroxidase). Enantiomeric substrates labeled with two different fluorescent dyes allow real‐time analysis of enantioselectivity by determination of the ratio of green and red single‐cell fluorescence.</description><subject>asymmetric catalysis</subject><subject>directed evolution</subject><subject>Directed Molecular Evolution</subject><subject>Drug Evaluation, Preclinical</subject><subject>enzyme catalysis</subject><subject>Escherichia coli - enzymology</subject><subject>Esterases - chemistry</subject><subject>Flow Cytometry</subject><subject>hydrolases</subject><subject>Hydrolysis</subject><subject>kinetic resolution</subject><subject>Models, Biological</subject><subject>Molecular Structure</subject><subject>Peroxidase - chemistry</subject><subject>Stereoisomerism</subject><subject>Surface Properties</subject><issn>1433-7851</issn><issn>1521-3773</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtv00AUha0K1BdsWYJX3TnMw_NaVlFIIlVlkYQsR5OZ62TAscOMTTG_vlM5KuxY3aN7v3Oke7LsA0YTjBD5bBoPE4KQQIxQfpFdY0ZwQYWgb5IuKS2EZPgqu4nxe-KlRPwyu8JpRwgS19lm5Zt9DcUU6jpf-P2hWB9C2-8Pp77LVzYANAnI122-dNB0vhryWWOSaCPUYDv_C_LF4EJbD5236fZnOEJ8l72tTB3h_XneZpsvs_V0UTx8nS-n9w-FLQXmhaN0h5WRTDi3c9IoljYl5gSpignLhQKQUlpRsQqVpSTKcYc4Uw4qKzint9ndmHsK7c8eYqePPtr0immg7aPmilBKOErgZARtaGMMUOlT8EcTBo2RfilSvxSpX4tMho_n5H53BPcXPzeXADUCT76G4T9x-v5xOfs3vBi9Pnbw-9Vrwg_NBRVMbx_nmm-38tuUlnqe-E8jX5lWm33wUW9WBGGKkMKIcUKfAbihl-s</recordid><startdate>20080623</startdate><enddate>20080623</enddate><creator>Becker, Stefan</creator><creator>Höbenreich, Horst</creator><creator>Vogel, Andreas</creator><creator>Knorr, Janina</creator><creator>Wilhelm, Susanne</creator><creator>Rosenau, Frank</creator><creator>Jaeger, Karl-Erich</creator><creator>Reetz, Manfred T</creator><creator>Kolmar, Harald</creator><general>Wiley-VCH Verlag</general><general>WILEY-VCH Verlag</general><general>WILEY‐VCH Verlag</general><scope>FBQ</scope><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20080623</creationdate><title>Single-Cell High-Throughput Screening To Identify Enantioselective Hydrolytic Enzymes</title><author>Becker, Stefan ; Höbenreich, Horst ; Vogel, Andreas ; Knorr, Janina ; Wilhelm, Susanne ; Rosenau, Frank ; Jaeger, Karl-Erich ; Reetz, Manfred T ; Kolmar, Harald</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4716-d33b19a857ddbd8a95d33416209f57c679ee888c7f5f044829d6d0659defc7663</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>asymmetric catalysis</topic><topic>directed evolution</topic><topic>Directed Molecular Evolution</topic><topic>Drug Evaluation, Preclinical</topic><topic>enzyme catalysis</topic><topic>Escherichia coli - enzymology</topic><topic>Esterases - chemistry</topic><topic>Flow Cytometry</topic><topic>hydrolases</topic><topic>Hydrolysis</topic><topic>kinetic resolution</topic><topic>Models, Biological</topic><topic>Molecular Structure</topic><topic>Peroxidase - chemistry</topic><topic>Stereoisomerism</topic><topic>Surface Properties</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Becker, Stefan</creatorcontrib><creatorcontrib>Höbenreich, Horst</creatorcontrib><creatorcontrib>Vogel, Andreas</creatorcontrib><creatorcontrib>Knorr, Janina</creatorcontrib><creatorcontrib>Wilhelm, Susanne</creatorcontrib><creatorcontrib>Rosenau, Frank</creatorcontrib><creatorcontrib>Jaeger, Karl-Erich</creatorcontrib><creatorcontrib>Reetz, Manfred T</creatorcontrib><creatorcontrib>Kolmar, Harald</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Angewandte Chemie (International ed.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Becker, Stefan</au><au>Höbenreich, Horst</au><au>Vogel, Andreas</au><au>Knorr, Janina</au><au>Wilhelm, Susanne</au><au>Rosenau, Frank</au><au>Jaeger, Karl-Erich</au><au>Reetz, Manfred T</au><au>Kolmar, Harald</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Single-Cell High-Throughput Screening To Identify Enantioselective Hydrolytic Enzymes</atitle><jtitle>Angewandte Chemie (International ed.)</jtitle><addtitle>Angewandte Chemie International Edition</addtitle><date>2008-06-23</date><risdate>2008</risdate><volume>47</volume><issue>27</issue><spage>5085</spage><epage>5088</epage><pages>5085-5088</pages><issn>1433-7851</issn><eissn>1521-3773</eissn><abstract>Getting a look in: A high‐throughput screening method has been developed for the identification and isolation of enantioselective hydrolases displayed on cell surfaces (see scheme; E: Esterase, P: Peroxidase). Enantiomeric substrates labeled with two different fluorescent dyes allow real‐time analysis of enantioselectivity by determination of the ratio of green and red single‐cell fluorescence.</abstract><cop>Weinheim</cop><pub>Wiley-VCH Verlag</pub><pmid>18512207</pmid><doi>10.1002/anie.200705236</doi><tpages>4</tpages></addata></record> |
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subjects | asymmetric catalysis directed evolution Directed Molecular Evolution Drug Evaluation, Preclinical enzyme catalysis Escherichia coli - enzymology Esterases - chemistry Flow Cytometry hydrolases Hydrolysis kinetic resolution Models, Biological Molecular Structure Peroxidase - chemistry Stereoisomerism Surface Properties |
title | Single-Cell High-Throughput Screening To Identify Enantioselective Hydrolytic Enzymes |
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